Protein Variants | Comment | Organism |
---|---|---|
A61V | 11.6fold increase in cyclic di-AMP production | Bacillus subtilis |
A76V | 4.3fold increase in cyclic di-AMP production | Bacillus subtilis |
E46K | 19.5fold increase in cyclic di-AMP production | Bacillus subtilis |
L44F | 90.5fold increase in cyclic di-AMP production | Bacillus subtilis |
additional information | very low expression of CdaS as the single diadenylate cyclase results in the appearance of spontaneous suppressor mutations. Several of these mutations in the cdaS gene affect the N-terminal domain of CdaS. The corresponding CdaS mutant proteins exhibit a significantly increased enzymatic activity. Deletion of the first or both N-terminal domain alpha-helices results also in strongly increased activity. The mutations and the deletions of the N-terminal domain result in conformational changes that lead to highly increased enzymatic activity. Although the full-length CdaS protein forms hexamers, a truncated version with a deletion of the first N-terminal helix formed dimers with high enzyme activity | Bacillus subtilis |
P201Q | 12.8fold increase in cyclic di-AMP production | Bacillus subtilis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
17000 | - |
and 37000 and 167000 Da, gel filtration | Bacillus subtilis |
23000 | - |
- |
Bacillus subtilis |
37000 | - |
and 167000 and 17000 Da, gel filtration | Bacillus subtilis |
167000 | - |
and 37000 and 17000 Da, gel filtration | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | O31854 | - |
- |
Bacillus subtilis 168 | O31854 | - |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 23000, calculated, plus hexamer and monomer | Bacillus subtilis |
hexamer | 6 * 23000, calculated, plus monomer and dimer | Bacillus subtilis |
monomer | 1 * 23000, calculated, plus hexamer and dimer | Bacillus subtilis |